ID   POA1_AJECN              Reviewed;         254 AA.
AC   A6QXU0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
GN   Name=POA1; ORFNames=HCAG_02197;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Highly specific phosphatase involved in the metabolism of
CC       ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of
CC       tRNA splicing. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-beta-D-ribose 1''-phosphate + H2O = ADP-D-ribose +
CC         phosphate; Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84;
CC   -!- SIMILARITY: Belongs to the POA1 family. {ECO:0000305}.
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DR   EMBL; CH476656; EDN05594.1; -; Genomic_DNA.
DR   RefSeq; XP_001542026.1; XM_001541976.1.
DR   AlphaFoldDB; A6QXU0; -.
DR   SMR; A6QXU0; -.
DR   STRING; 339724.A6QXU0; -.
DR   EnsemblFungi; EDN05594; EDN05594; HCAG_02197.
DR   GeneID; 5448812; -.
DR   KEGG; aje:HCAG_02197; -.
DR   VEuPathDB; FungiDB:HCAG_02197; -.
DR   HOGENOM; CLU_054419_1_0_1; -.
DR   OMA; NCQGSWG; -.
DR   OrthoDB; 1416296at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.220.10; -; 1.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   Pfam; PF01661; Macro; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..254
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324900"
FT   DOMAIN          1..254
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   REGION          86..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9..11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         23..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         30..35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220..226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   254 AA;  27451 MW;  5A7369A8896A5CF2 CRC64;
     MSIITEIQGD LFDAPEGAAL IHACNCQGSW GKGIAATFKE KYPAAYRIFR SHCQQYLSHP
     QTWTQTQTSR QQSRAFKLPE GTALIIPPQP ADYQPQPQPQ SQTAPLSNCG RGRGRGRGRA
     GGGALHNSRE LTALSRPAGK KHWIICLFTS WHYGRWSRSP PDIILENTMS AMADLKRQIA
     AAAAASSTTS PATTTTTTTA LAATGGCEEE QLGELWGCRL NAGLFEVPWE RTKAVLEEAG
     LAVTIVQPPG SGYE